English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Entropically driven Polymeric Enzyme Inhibitors by End‐Group directed Conjugation

MPS-Authors
/persons/resource/persons58388

Alachraf,  Mohammed Wasim
Service Department Schrader (MS), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

/persons/resource/persons58974

Schrader,  Wolfgang
Service Department Schrader (MS), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Hijazi, M., Krumm, C., Cinar, S., Arns, L., Alachraf, M. W., Hiller, W., et al. (2018). Entropically driven Polymeric Enzyme Inhibitors by End‐Group directed Conjugation. Chemistry – A European Journal, 24(18), 4523-4527. doi:10.1002/chem.201800168.


Cite as: http://hdl.handle.net/21.11116/0000-0001-7069-B
Abstract
A new generic concept for polymeric enzyme inhibitors is presented using the example of poly(2‐methyl‐2‐oxazoline) (PMOx) terminated with an iminodiacetate (IDA) function. These polymers are shown to be non‐competitive inhibitors for horseradish peroxidase (HRP). Mechanistic investigations revealed that the polymer is directed to the protein by its end group and collapses at the surface in an entropy‐driven process as shown by isothermal titration calorimetry. The dissociation constant of the complex was determined as the inhibition constant Ki using HRP kinetic activity measurements. Additional experiments suggest that the polymer does not form a diffusion layer around the protein, but might inhibit by inducing minor conformational changes in the protein. This kind of inhibitor offers new avenues towards designing bioactive compounds.